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On the Conformational Stability of Globular Proteins
Open accessAbstract
This article describes research into the conformational stability of globular proteins -- specifically the effects of various electrolytes and nonelectrolytes on the thermally induced structural transition in ribonuclease. Optical rotatory methods were used to measure transition parameters including: melting temperature (T m ), the size of the transition (DELTA(alpha)), its breadth, and the specific optical rotation and optical rotary dispersion of the pre- and post-transition compounds. Structural perturbants investigated were neutral salts (with and without ethylene glycol), urea and the guanidinium salts, the tetraalkylammonium ions and the alcohols. Physicochemical instrumental analysis methods used in the study include polarimetry, viscometry, ultraviolet (UV) spectroscopy, short column sedimentation (weight average molecular weights); spectrophotometry and interferometry were used to characterize the bovine pancreatic ribonuclease used for most of the experiments.
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Cited by
Interactions of macromolecules with salt ions: An electrostatic theory for the Hofmeister effect
Zhou, H. (2005) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.20500 · Cited by 72
Effect of heating at 56°C on mouse IgE antibodies
Prouvost-Danon, A., Binaghi, R. A., & Abadie, A. (1977) · Immunochemistry · doi:10.1016/0019-2791(77)90284-1 · Cited by 22
Metadata
- Authors
- von Hippel, P. H., & Wong, K.-Y.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1965-10
- Volume
- 240
- Issue
- 10
- Pages
- 3909-3923
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W114418772
- Cited by
- 518
- References
- 0
- FWCI
- 6.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- von Hippel, P. H., & Wong, K.-Y. (1965). On the Conformational Stability of Globular Proteins. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)97128-0
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
